Structure of PDB 5okg Chain B

Receptor sequence
>5okgB (length=462) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
RHLKPFPPEFLWGAASAAYQVEGAWNEDGKGLSVWDVFAKQPGRTFKGTN
GDVAVDHYHRYQEDVALMAEMGLKAYRFSVSWSRVFPDGNGAVNEKGLDF
YDRLIEELRNHGIEPIVTLYHWDVPQALMDAYGAWESRRIIDDFDRYAVT
LFQRFGDRVKYWVTLNQQNIFISFGYRLGLHPPGVKDMKRMYEANHIANL
ANAKVIQSFRHYVPDGKIGPSFAYSPMYPYDSRPENVLAFENAEEFQNHW
WMDVYAWGMYPQAAWNYLESQGLEPTVAPGDWELLQAAKPDFMGVNYYQT
TTVEHNPPDGVGTSSGIPGLFKTVRNPHVDTTNWDWAIDPVGLRIGLRRI
ANRYQLPILITENGLGEFDTLEPGDIVNDDYRIDYLRRHVQEIQRAITDG
VDVLGYCAWSFTDLLSWLNGYQKRYGFVYVNRDDESEKDLRRIKKKSFYW
YQRVIETNGAEL
3D structure
PDB5okg Structural basis for enzyme bifunctionality - the case of Gan1D from Geobacillus stearothermophilus.
ChainB
Resolution1.25 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R80 H124 Q170 I173 N299 Y301 E378
Catalytic site (residue number reindexed from 1) R77 H121 Q167 I170 N296 Y298 E362
Enzyme Commision number 3.2.1.85: 6-phospho-beta-galactosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 BG6 B Q23 Q170 E378 W425 Y441 Q20 Q167 E362 W409 Y425
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033920 6-phospho-beta-galactosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5okg, PDBe:5okg, PDBj:5okg
PDBsum5okg
PubMed28975708
UniProtW8QF82

[Back to BioLiP]